› 1dbi

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE

Released:
DOI: 10.2210/pdb1dbi/pdb
PDB entry 1dbi coloured by chain, front view.
PDB entry 1dbi coloured by chain, side view.
PDB entry 1dbi coloured by chain, top view.
Source organism: Bacillus sp. Ak1
Primary publication:
Calcium-mediated thermostability in the subtilisin superfamily: the crystal structure of Bacillus Ak.1 protease at 1.8 A resolution.
Smith CA, Toogood HS, Baker HM, Daniel RM, Baker EN
J Mol Biol 294 1027-40 (1999)
PMID: 10588904

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175069 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermophilic serine proteinase Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 29.79 KDa
Source organism: Bacillus sp. Ak1
UniProt:
  • Canonical: Q45670 (Residues: 122-401; Coverage: 74%)
Sequence domains: Subtilase family
Structure domains: Peptidase S8/S53 domain

Ligands and Environments

2 bound ligands:
Ligand CA 3 x CA
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 44.05Å b: 51.68Å c: 52.78Å
α: 90° β: 96.1° γ: 90°
R-values:
R R work R free
0.182 0.182 0.247

Quick links

Citations

5 review citations

Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability.
Vieille et al. (2001)
4 more

16 mentions without citation

Insights from bacterial subtilases into the mechanisms of intramolecular chaperone-mediated activation of furin.
Shinde et al. (2011)
15 more